A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis
A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis
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DOI：
10.1016/j.febslet.2012.02.019
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发表时间：
2012-03-23
期刊：
影响因子：
3.5
通讯作者：
Takano, Tetsuo
中科院分区：
文献类型：
--
作者：
Tsugama, Daisuke;Liu, Shenkui;Takano, Tetsuo
N-肉豆蔻酰化是许多信号蛋白的脂质修饰，其中肉豆蔻酸被添加到N-末端甘氨酸残基。在这里，我们表明，PP 2C 74，一个假定的豆蔻酰化的2C型蛋白磷酸酶（PP 2C）在拟南芥，在各种组织中转录，并具有蛋白磷酸酶活性。GFP融合的PP 2C 74定位于质膜，但不是当甘氨酸残基在位置2，这是推定的豆蔻酰化位点，被取代为丙氨酸残基。酵母双杂交分析和GST下拉分析表明，PP 2C 74与AKIN 10相互作用，AKIN 10是SnRK 1蛋白激酶复合物的催化α亚基，其β亚基是豆蔻酰化的已知靶点。蛋白质相互作用的结构化总结：AKIN 10通过双杂交与PP 2C 74物理相互作用（查看相互作用）AKIN 10通过下拉与PP 2C 74物理相互作用（查看相互作用）（C）2012欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
N-myristoylation is a lipid modification of many signaling proteins in which myristate is added to an N-terminal glycine residue. Here we show that PP2C74, a putative myristoylated 2C-type protein phosphatase (PP2C) in Arabidopsis, is transcribed in various tissues and has protein phosphatase activity. GFP-fused PP2C74 localized to the plasma membrane, but not when a glycine residue at position 2, which is the putative myristoylation site, was substituted with an alanine residue. Yeast two-hybrid analysis and GST pull-down analysis showed that PP2C74 interacts with AKIN10, the catalytic alpha subunit of the SnRK1 protein kinase complex, the beta subunits of which are known targets of myristoylation.Structured summary of protein interactions:AKIN10 physically interacts with PP2C74 by two hybrid (View interaction)AKIN10 physically interacts with PP2C74 by pull down (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.